ID A0A168HRZ7_CORDF Unreviewed; 806 AA.
AC A0A168HRZ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Splicing factor u2af large subunit {ECO:0000313|EMBL:OAA78157.1};
GN ORFNames=LEL_04980 {ECO:0000313|EMBL:OAA78157.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78157.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA78157.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78157.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS15 family.
CC {ECO:0000256|ARBA:ARBA00008434}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA78157.1}.
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DR EMBL; AZHF01000003; OAA78157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168HRZ7; -.
DR STRING; 1081108.A0A168HRZ7; -.
DR OrthoDB; 101932at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProt.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00353; Ribosomal_S15p_S13e; 1.
DR CDD; cd12232; RRM3_U2AF65; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR Gene3D; 4.10.860.130; -; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000589; Ribosomal_uS15.
DR InterPro; IPR023029; Ribosomal_uS15_arc_euk.
DR InterPro; IPR012606; Ribosomal_uS15_N.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR PANTHER; PTHR23139; RNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR23139:SF9; SPLICING FACTOR U2AF 65 KDA SUBUNIT; 1.
DR Pfam; PF08069; Ribosomal_S13_N; 1.
DR Pfam; PF00312; Ribosomal_S15; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM01386; Ribosomal_S13_N; 1.
DR SMART; SM01387; Ribosomal_S15; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS00362; RIBOSOMAL_S15; 1.
DR PROSITE; PS50102; RRM; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 264..347
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 373..469
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 498..589
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 89296 MW; BF03C108D4B3AC04 CRC64;
MNGDNYSSRG ESVVSSGKHP NADGMLAAKE GDNRRDHQSS RGERGERGER GDRSDRGDRR
DRGDDRRDRH RDRRRSRSPH DRHRRDRDRD GDAYASSRNH RDREREERYQ GGGGRERRGD
REWDRDRGSS RRDARRDDDG HGRRDRDGFD DQRRGGRERR DDGFARQQER RSPSPPKRRE
PTPDLTDIIP VLERKRRMTQ WDIKPPGYEA VTSEQAKMSG MFPLPGAPRQ QQMDPSKLQA
FINQPAGGQV SSAGLKASNS RQAKRLLVSN LPRGTTDGAL VAFFNLQLNG LNVIEATDPC
ALSQLSNDNS FAVLEFKNTG DATTALALDG ISMVADTPGI SIRRPKDYVM PAVPEDVIYN
PEVVSNAVPD TIHKLCLTNI PPFLTEDQVL ELLAAFGKPK AFVLVKDRST EESRVCNPYP
SATAFALTEN QGIAFAEYAD PGSANEPALN TLNGMDVGGK KLKVVKACVG GTQVANFDAG
INAISNLAGQ GNGGEATRVL QLLNMVTAEE LLDNDDYEEI CDDVRDECSK YGKILDIKVP
RPAGGSRQSA GVGRIFVKFE SADSTTSALK ALAGRKFADR TVVTTYFPEE NFDVSACSHD
EHTTHKSALT KRKFAPLHNL SPVFVLPSQT SLRSPGKLHH DSSNLNTRQP TTTDNMGRLH
SNGKGISASA LPYSRTAPSW LKTTPEQVVE QICKLARKGA TPSQIGVILR DSHGVSQVKL
VTGNRILRIL KSSGLAPELP EDLYMLIKKA VAVRKHLERN RKDKDSKFRL ILIESRIHRL
ARYYKTVGVL PPTWKYESAT ASTIVA
//
